| UniProt functional annotation for Q1GNW5 | |||
| UniProt code: Q1GNW5. |
| Organism: | Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis). | |
| Taxonomy: | Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingopyxis. | |
| Function: | Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2- oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine. {ECO:0000269|PubMed:24714029, ECO:0000269|PubMed:25172507}. | |
| Catalytic activity: | Reaction=2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 + succinate; Xref=Rhea:RHEA:45740, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58515, ChEBI:CHEBI:85413; EC=1.14.11.55; Evidence={ECO:0000269|PubMed:24714029, ECO:0000269|PubMed:25172507}; | |
| Cofactor: | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:24714029, ECO:0000269|PubMed:25172507}; Note=Binds 1 Fe(2+) ion. {ECO:0000269|PubMed:24714029, ECO:0000269|PubMed:25172507}; | |
| Biophysicochemical properties: | Kinetic parameters: KM=2.7 mM for 2-oxoglutarate (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:24714029}; KM=9.8 mM for ectoine (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:24714029}; Vmax=1 umol/min/mg enzyme (at pH 8 and 40 degrees Celsius) {ECO:0000269|PubMed:24714029}; Note=Kcat is 1.2 sec(-1) for ectoin as substrate (at pH 8 and 40 degrees Celsius). {ECO:0000269|PubMed:24714029}; pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:24714029}; Temperature dependence: Optimum temperature is 40 degrees Celsius (PubMed:24714029). Active from 5 to 50 degrees Celsius (PubMed:24714029). {ECO:0000269|PubMed:24714029}; | |
| Subunit: | Homodimer. {ECO:0000269|PubMed:24714029, ECO:0000269|PubMed:25172507}. | |
| Similarity: | Belongs to the PhyH family. EctD subfamily. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.